Abstract
The covalent attachment of Fab‘ fragments of polyclonal anti-human IgG to a polymerizable lipid with a terminal linker group (N-(e-maleimidocaproyl)dilinoleoylphosphatidylethanolamine) was examined by means of quartz crystal microbalance (QCM), surface plasmon resonance (SPR), and atomic force microscopy (AFM). The linker lipid was embedded in a monolayer of dilinoleoylphosphatidylethanolamine. Both monomeric and cross-linked biofunctionalized monolayers were studied. Atomic force microscope images showed that the monomeric monolayer consisted of large holes when it was deposited on a solid substrate, while the cross-linked monolayer appeared as a planar two-dimensional film. The ability of the biofunctionalized monolayer to bind proteins decreased with UV-irradiation time. However, an increase in the linker lipid concentration in the lipid matrix increased the protein-binding efficiency. A comparison between QCM and SPR measurements indicated that the QCM measurements overestimated the binding efficiency...
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